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Literature summary extracted from

  • Fan, F.; Ghanem, M.; Gadda, G.
    Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance (2004), Arch. Biochem. Biophys., 421, 149-158.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.17 0.6
-
choline pH 7.0, 25°C Arthrobacter globiformis
1.1.3.17 2.3
-
betaine-aldehyde pH 7.0, 25°C Arthrobacter globiformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.17 60612
-
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis
1.1.3.17 60614
-
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis
1.1.3.17 117000 122000 gel filtration Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.17 Arthrobacter globiformis Q7X2H8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.17 recombinant enzyme, expression in Escherichia coli Arthrobacter globiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.17 betaine aldehyde + O2 + H2O
-
Arthrobacter globiformis betaine + H2O2
-
?
1.1.3.17 choline + O2
-
Arthrobacter globiformis betaine aldehyde + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.1.3.17 dimer 2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.17 11.6
-
betaine-aldehyde pH 7.0, 25°C Arthrobacter globiformis
1.1.3.17 13.4
-
choline pH 7.0, 25°C Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.17 FAD one moiety per enzyme monomer, covalently bound Arthrobacter globiformis